(data stored in ACNUC7421 zone)

SWISSPROT: PAND_ECO27

ID   PAND_ECO27              Reviewed;         126 AA.
AC   B7UIH9;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 54.
DE   RecName: Full=Aspartate 1-decarboxylase {ECO:0000255|HAMAP-Rule:MF_00446};
DE            EC=4.1.1.11 {ECO:0000255|HAMAP-Rule:MF_00446};
DE   AltName: Full=Aspartate alpha-decarboxylase {ECO:0000255|HAMAP-Rule:MF_00446};
DE   Contains:
DE     RecName: Full=Aspartate 1-decarboxylase beta chain {ECO:0000255|HAMAP-Rule:MF_00446};
DE   Contains:
DE     RecName: Full=Aspartate 1-decarboxylase alpha chain {ECO:0000255|HAMAP-Rule:MF_00446};
DE   Flags: Precursor;
GN   Name=panD {ECO:0000255|HAMAP-Rule:MF_00446};
GN   OrderedLocusNames=E2348C_0134;
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC;
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
CC   -!- FUNCTION: Catalyzes the pyruvoyl-dependent decarboxylation of
CC       aspartate to produce beta-alanine. {ECO:0000255|HAMAP-
CC       Rule:MF_00446}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + L-aspartate = beta-alanine + CO2;
CC         Xref=Rhea:RHEA:19497, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:29991, ChEBI:CHEBI:57966; EC=4.1.1.11;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00446};
CC   -!- COFACTOR:
CC       Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00446};
CC       Note=Binds 1 pyruvoyl group covalently per subunit.
CC       {ECO:0000255|HAMAP-Rule:MF_00446};
CC   -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis;
CC       beta-alanine from L-aspartate: step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_00446}.
CC   -!- SUBUNIT: Heterooctamer of four alpha and four beta subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00446}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00446}.
CC   -!- PTM: Is synthesized initially as an inactive proenzyme, which is
CC       activated by self-cleavage at a specific serine bond to produce a
CC       beta-subunit with a hydroxyl group at its C-terminus and an alpha-
CC       subunit with a pyruvoyl group at its N-terminus.
CC       {ECO:0000255|HAMAP-Rule:MF_00446}.
CC   -!- SIMILARITY: Belongs to the PanD family. {ECO:0000255|HAMAP-
CC       Rule:MF_00446}.
DR   EMBL; FM180568; CAS07682.1; -; Genomic_DNA.
DR   RefSeq; WP_000621515.1; NC_011601.1.
DR   SMR; B7UIH9; -.
DR   EnsemblBacteria; CAS07682; CAS07682; E2348C_0134.
DR   KEGG; ecg:E2348C_0134; -.
DR   KO; K01579; -.
DR   OMA; LYSKIHR; -.
DR   BioCyc; ECOL574521:E2348C_RS00690-MONOMER; -.
DR   UniPathway; UPA00028; UER00002.
DR   Proteomes; UP000008205; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004068; F:aspartate 1-decarboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006523; P:alanine biosynthetic process; IEA:InterPro.
DR   GO; GO:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd06919; Asp_decarbox; 1.
DR   HAMAP; MF_00446; PanD; 1.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR003190; Asp_decarbox.
DR   PANTHER; PTHR21012; PTHR21012; 1.
DR   Pfam; PF02261; Asp_decarbox; 1.
DR   PIRSF; PIRSF006246; Asp_decarbox; 1.
DR   ProDom; PD009294; Asp_decarbox; 1.
DR   SUPFAM; SSF50692; SSF50692; 1.
DR   TIGRFAMs; TIGR00223; panD; 1.
PE   3: Inferred from homology;
DR   PRODOM; B7UIH9.
DR   SWISS-2DPAGE; B7UIH9.
KW   Autocatalytic cleavage; Complete proteome; Cytoplasm; Decarboxylase;
KW   Lyase; Pantothenate biosynthesis; Pyruvate; Schiff base; Zymogen.
FT   CHAIN         1     24       Aspartate 1-decarboxylase beta chain.
FT                                {ECO:0000255|HAMAP-Rule:MF_00446}.
FT                                /FTId=PRO_1000191993.
FT   CHAIN        25    126       Aspartate 1-decarboxylase alpha chain.
FT                                {ECO:0000255|HAMAP-Rule:MF_00446}.
FT                                /FTId=PRO_1000191994.
FT   REGION       73     75       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00446}.
FT   ACT_SITE     25     25       Schiff-base intermediate with substrate;
FT                                via pyruvic acid. {ECO:0000255|HAMAP-
FT                                Rule:MF_00446}.
FT   ACT_SITE     58     58       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00446}.
FT   BINDING      57     57       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00446}.
FT   MOD_RES      25     25       Pyruvic acid (Ser). {ECO:0000255|HAMAP-
FT                                Rule:MF_00446}.
SQ   SEQUENCE   126 AA;  13834 MW;  E3169F5C2BDD5D25 CRC64;
     MIRTMLQGKL HRVKVTHADL HYEGSCAIDQ DFLDAAGILE NEAIDIWNVT NGKRFSTYAI
     AAERGSRIIS VNGAAAHCAS VGDIVIIASF VTMPDEEART WRPNVAYFEG DNEMKRTAKA
     IPVQVA
//

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